7NH5
Co-Crystal Structure of Akt1 in Complex with Covalent-Allosteric Akt Inhibitor 6
Summary for 7NH5
Entry DOI | 10.2210/pdb7nh5/pdb |
Descriptor | RAC-alpha serine/threonine-protein kinase, ACETATE ION, ~{N}-methyl-6-[4-[[4-[2-oxidanylidene-6-(propanoylamino)-3~{H}-benzimidazol-1-yl]piperidin-1-yl]methyl]phenyl]-5-phenyl-pyridine-3-carboxamide, ... (4 entities in total) |
Functional Keywords | akt1, akt2, akt3, covalent-allosteric, transferase |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 1 |
Total formula weight | 52393.78 |
Authors | Landel, I.,Mueller, M.P.,Rauh, D. (deposition date: 2021-02-10, release date: 2021-09-08, Last modification date: 2024-01-31) |
Primary citation | Quambusch, L.,Depta, L.,Landel, I.,Lubeck, M.,Kirschner, T.,Nabert, J.,Uhlenbrock, N.,Weisner, J.,Kostka, M.,Levy, L.M.,Schultz-Fademrecht, C.,Glanemann, F.,Althoff, K.,Muller, M.P.,Siveke, J.T.,Rauh, D. Cellular model system to dissect the isoform-selectivity of Akt inhibitors. Nat Commun, 12:5297-5297, 2021 Cited by PubMed: 34489430DOI: 10.1038/s41467-021-25512-8 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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